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Literature summary for 4.2.1.20 extracted from

  • Osborne, A.; Teng, Q.; Miles, E.W.; Phillips, R.S.
    Detection of Open and Closed Conformations of Tryptophan Synthase by 15N-Heteronuclear Single-Quantum Coherence Nuclear Magnetic Resonance of Bound 1-15N-L-Tryptophan (2003), J. Biol. Chem., 278, 44083-44090.
    View publication on PubMed
Search for more literature for 4.2.1.20

Protein Variants

Protein Variants Comment Organism
D305A mutation of a beta-subunit residue, no active site residue, altered subunit interaction Escherichia coli
E109D mutation of a beta-subunit active site residue, reduced reach and conformational freedom of the carboxylate functionality, accumulation of indole at the beta-site Escherichia coli
K87T mutation of a beta-subunit active site residue, inactive mutant, which can form an external aldimine, but cannot form an alpha-aminoacrylate intermediate Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8) Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(indol-3-yl)glycerol 3-phosphate alpha-subunit of the bienzyme complex, alpha-reaction Escherichia coli D-glyceraldehyde 3-phosphate + indole
-
 ?
L-serine + indole beta-subunit of the bienzyme complex, beta-reaction Escherichia coli L-tryptophan + H2O
-
 ?
additional information enzyme switches between open inactive conformation and closed active conformation, overview Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More NMR measurement and determination of wild-type and mutant enzyme structures, complexed with L-tryptophane, in presence or absence of allosteric ligands, such as Na+, NH4+, Cs+, and DL_alpha-glycerol 3-phosphate, overview Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli